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Lipids and Lipid Metabolism in Postnatal Gut Development and Risk of Intestinal Injury
Published in David J. Hackam, Necrotizing Enterocolitis, 2021
Utilization of fatty acids at the cellular level begins with internalization of the fatty acid into the cell via fatty acid transporters. Once within the cell, the fatty acid is converted to fatty acyl-CoA via fatty acyl-CoA synthase (Figure 49.2). At the outer membrane of the mitochondria, carnitine palmitoyltransferase 1 converts the fatty acid-CoA to fatty acyl carnitine. Fatty acyl carnitine then crosses the inner mitochondrial membrane through a carnitine exchange via carnitine-acyl carnitine translocase. Once inside the mitochondrial matrix, the fatty acyl carnitine is converted back to fatty acyl-CoA via carnitine palmitoyltransferase 2, allowing for entry into the β-oxidation pathway generating acetyl-CoA. Acetyl-CoA is utilized by the tricarboxylic acid cycle (TCA) cycle to form NADH and FADH2.
The effect of Telmisartan on lipid levels and proinflammatory cytokines in ESRD patients undergoing hemodialysis
Published in Elida Zairina, Junaidi Khotib, Chrismawan Ardianto, Syed Azhar Syed Sulaiman, Charles D. Sands, Timothy E. Welty, Unity in Diversity and the Standardisation of Clinical Pharmacy Services, 2017
B. Suprapti, W.P. Nilamsari, Z. Izzah, M. Dhrik, B. Dharma
The activation of PPARƔ increases the expression of many kinds of genes as well as enzymes related to carbohydrate metabolism (adiponectine, glucokinase, GLUT-4 glucose transporter) and lipid metabolism (lipoprotein lipase, adipocyte fatty acid transporter protein, fatty acyl CoA synthase, malic enzyme). Likewise, the activation of PPARƔ suppresses the activity of inflammatory factor TNF-α, which suppresses insulin sensitivity through insulin signal transduction disorders (Bouskila et al. 2005).
Current and emerging gluconeogenesis inhibitors for the treatment of Type 2 diabetes
Published in Expert Opinion on Pharmacotherapy, 2021
The fibrates are clinically approved inhibitors of PPAR-α and activate multiple genes involved in lipoprotein transport. Fibrates are used to lower triglyceride levels. The thiazolidinediones have been effective hypoglycemic agents. Their effect is on PPAR-γ, at least in part through reduction of fatty acid release and promotion of fatty acid oxidation, thus improving insulin sensitivity [102–104]. Activation of PPAR-γ alters the transcription of multiple genes involved in glucose and lipid metabolism including lipoprotein lipase, fatty acid transporter protein, adipocyte fatty-acid-binding protein, fatty acyl-CoA synthase, malic enzyme, glucokinase, and the GLUT4 glucose transporter.
Vascular endothelial growth factor B inhibits lipid accumulation in C2C12 myotubes incubated with fatty acids
Published in Growth Factors, 2019
Ling-Jie Li, Jin Ma, Song-Bo Li, Xuefei Chen, Jing Zhang
There are three types of fatty acid transporters on the skeletal muscle cell surface: fatty acid translocase (FAT/CD36), FATP, and FABP (Huang et al. 2018; Lukaszuk et al. 2012). FATP1 and FATP4 are two subtypes of FATP specifically expressed in skeletal muscle (Baati et al. 2017). Our work indicates that low concentrations of VEGFB significantly upregulated skeletal-muscle FATP1 and FATP4 but had no effect on FAT/CD36 or other FABP subtypes. Single treatment with VEGF-B only without fatty acids had no effect on CD36, FATP1 and FATP4 (see Supplementary 4). These results are similar to the regulatory effect of VEGFB on endothelial-cell FATP expression (Hagberg et al. 2010; Elias et al. 2012; Mehlem et al. 2016). In vitro, VEGFB-167 and VEGFB-186 greatly promoted endothelial-cell FATP3 and FATP4 expression in cultured endothelial cells (Hagberg et al. 2010). In vivo, mice with VEGFB-186 adenovirus and VEGFB transgenic mice both showed increased myocardial FATP3 and FATP4 expression, and VEGFB–/– inhibited FATP3 and FATP4 expression (Hagberg et al. 2010, 2013; Kivelä et al. 2014; Li 2010; Falkevall et al. 2017). These results demonstrate that VEGFB specifically regulates FATP expression in endothelial cells and skeletal muscle cells. However, whether increased expression of FATP indicates increased fatty acid uptake is unknown. In endothelial cells treated with VEGFB, lipid accumulation depends on FATP3 or FATP4 expression (Hagberg et al. 2010); however, FATP4 expression was increased in a cardiac-specific VEGFB-overexpression model, but changes in LCFA uptake were not investigated (Kivelä et al. 2014). Recent evidence suggests that FATP4 is in fact a fatty acyl-CoA synthase that resides in the endoplasmic reticulum, rather than a fatty acid transporter on the plasma membrane (Schneider et al. 2014; Lenz et al. 2011). In our study, we found that in addition to a significant increase in FATP4 expression with VEGFB, FATP1 expression was also increased ∼15-fold, so it plays an important role in skeletal muscle lipid uptake.